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UniProtKB/Swiss-Prot entry P29459


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IL12A_HUMAN
Primary accession number P29459
Secondary accession number Q96QZ1
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on January 23, 2002 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 84)
Name and origin of the protein
Protein name Interleukin-12 subunit alpha [Precursor]
Synonyms IL-12A
IL-12 subunit p35
Cytotoxic lymphocyte maturation factor 35 kDa subunit
CLMF p35
NK cell stimulatory factor chain 1
NKSF1
Gene name
Name: IL12A
Synonyms: NKSF1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1674604 [NCBI, ExPASy, EBI, Israel, Japan]
Gubler U., Chua A.O., Schoenhaut D.S., Dwyer C.M., McComas W., Motyka R., Nabavi N., Wolitzky A.G., Quinn P.M., Familletti P.C., Gately M.K.;
"Coexpression of two distinct genes is required to generate secreted bioactive cytotoxic lymphocyte maturation factor.";
Proc. Natl. Acad. Sci. U.S.A. 88:4143-4147(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1673147 [NCBI, ExPASy, EBI, Israel, Japan]
Wolf S.F., Temple P.A., Kobayashi M., Young D., Dicig M., Lowe L., Dzialo R., Fitz L., Ferenz C., Hewick R.M., Kelleher K., Herrmann S.H., Clark S.C., Azzoni L., Chan S.H., Trinchieri G., Perussia B.;
"Cloning of cDNA for natural killer cell stimulatory factor, a heterodimeric cytokine with multiple biologic effects on T and natural killer cells.";
J. Immunol. 146:3074-3081(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs program for genomic applications;
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 23-48.
PubMed=2204066 [NCBI, ExPASy, EBI, Israel, Japan]
Stern A.S., Podlaski F.J., Hulmes J.D., Pan Y.C.E., Quinn P.M., Wolitzky A.G., Familletti P.C., Stremlo D.L., Truitt T., Chizzonite R., Gately M.K.;
"Purification to homogeneity and partial characterization of cytotoxic lymphocyte maturation factor from human B-lymphoblastoid cells.";
Proc. Natl. Acad. Sci. U.S.A. 87:6808-6812(1990).
[5]
SIMILARITY TO IL-6.
DOI=10.1016/0167-5699(92)90140-3; PubMed=1374259 [NCBI, ExPASy, EBI, Israel, Japan]
Merberg D.M., Wolf S.F., Clark S.C.;
"Sequence similarity between NKSF and the IL-6/G-CSF family.";
Immunol. Today 13:77-78(1992).
[6]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 23-219, AND DISULFIDE BONDS.
DOI=10.1093/emboj/19.14.3530; PubMed=10899108 [NCBI, ExPASy, EBI, Israel, Japan]
Yoon C., Johnston S.C., Tang J., Stahl M., Tobin J.F., Somers W.S.;
"Charged residues dominate a unique interlocking topography in the heterodimeric cytokine interleukin-12.";
EMBO J. 19:3530-3541(2000).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M65271; AAA35694.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M65291; AAA59937.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF404773; AAK84425.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_000873.2; -.
UniGene Hs.673
3D structure databases
PDB
1F45; X-ray; 2.80 A; B=23-219.[ExPASy / RCSB / EBI]
PDBsum 1F45; -.
ModBase P29459.
Protein-protein interaction databases
DIP DIP:3772N; -.
IntAct P29459; -.
Organism-specific databases
H-InvDB HIX0030715; -.
HGNC HGNC:5969; IL12A.
GenAtlas IL12A.
HPA HPA001886; -.
MIM 161560; gene. [NCBI / EBI]
PharmGKB PA29784; -.
GeneCards P29459.
Gene expression databases
ArrayExpress P29459; -.
CleanEx HS_IL12A; -.
Ontologies
GO
GO:0043514; Cellular component: interleukin-12 complex (inferred from direct assay from UniProtKB).
GO:0005143; Molecular function: interleukin-12 receptor binding (non-traceable author statement from UniProtKB).
GO:0045513; Molecular function: interleukin-27 binding (inferred from physical interaction from UniProtKB).
GO:0046982; Molecular function: protein heterodimerization activity (inferred from physical interaction from UniProtKB).
GO:0007050; Biological process: cell cycle arrest (inferred from direct assay from UniProtKB).
GO:0016477; Biological process: cell migration (inferred from direct assay from UniProtKB).
GO:0050830; Biological process: defense response to Gram-positive bacterium (inferred from expression pattern from UniProtKB).
GO:0048662; Biological process: negative regulation of smooth muscle cell proliferation (inferred from direct assay from UniProtKB).
GO:0045785; Biological process: positive regulation of cell adhesion (inferred from direct assay from UniProtKB).
GO:0032729; Biological process: positive regulation of interferon-gamma production (inferred from direct assay from UniProtKB).
GO:0050671; Biological process: positive regulation of lymphocyte proliferation (inferred from direct assay from UniProtKB).
GO:0002860; Biological process: positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target (inferred from direct assay from UniProtKB).
GO:0032816; Biological process: positive regulation of natural killer cell activation (inferred from direct assay from UniProtKB).
GO:0034393; Biological process: positive regulation of smooth muscle cell apoptosis (inferred from direct assay from UniProtKB).
GO:0001916; Biological process: positive regulation of T cell mediated cytotoxicity (inferred from direct assay from UniProtKB).
GO:0042520; Biological process: positive regulation of tyrosine phosphorylation of Stat4 protein (inferred from direct assay from UniProtKB).
GO:0032496; Biological process: response to lipopolysaccharide (inferred from direct assay from UniProtKB).
GO:0010224; Biological process: response to UV-B (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR012351; 4_helix_cytokine_core.
IPR004281; IL12.
Graphical view of domain structure.
Gene3D G3DSA:1.20.1250.10; 4_helix_cytokine_core; 1.
PANTHER PTHR10523; IL12; 1.
Pfam PF03039; IL12; 1.
Pfam graphical view of domain structure.
BLOCKS P29459.
ProtoNet P29459.
Genome annotation databases
Ensembl ENSG00000168811; Homo sapiens. [Contig view]
GeneID 3592; -.
KEGG hsa:3592; -.
Phylogenomic databases
HOVERGEN P29459; -.
Other
NextBio 14035; -.
SOURCE IL12A; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytokine; Direct protein sequencing; Glycoprotein; Growth factor; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    22  22      
CHAIN   23   219  197     Interleukin-12 subunit alpha. PRO_0000015604
CARBOHYD   93    93        N-linked (GlcNAc...) (Potential). 
CARBOHYD   107   107        N-linked (GlcNAc...) (Potential). 
DISULFID   64   196         
DISULFID   85   123         
DISULFID   96    96        Interchain (with C-199 in IL12B). 
CONFLICT   213   213        M -> T (in Ref. 1; AAA35694). 
HELIX   43    58  16      
HELIX   59    61  3      
HELIX   81    84  4      
HELIX   88    92  5      
HELIX   118   145  28      
HELIX   155   169  15      
HELIX   190   217  28      
Sequence information
Length: 219 AA [This is the length of the unprocessed precursor] Molecular weight: 24874 Da [This is the MW of the unprocessed precursor] CRC64: 7C658AB7716112B2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MCPARSLLLV ATLVLLDHLS LARNLPVATP DPGMFPCLHH SQNLLRAVSN MLQKARQTLE 

        70         80         90        100        110        120 
FYPCTSEEID HEDITKDKTS TVEACLPLEL TKNESCLNSR ETSFITNGSC LASRKTSFMM 

       130        140        150        160        170        180 
ALCLSSIYED LKMYQVEFKT MNAKLLMDPK RQIFLDQNML AVIDELMQAL NFNSETVPQK 

       190        200        210 
SSLEEPDFYK TKIKLCILLH AFRIRAVTID RVMSYLNAS 

P29459 in FASTA format

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